ID F4TH01_ECOLX Unreviewed; 505 AA.
AC F4TH01;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01931};
DE Short=ATase {ECO:0000256|HAMAP-Rule:MF_01931};
DE EC=2.4.2.14 {ECO:0000256|HAMAP-Rule:MF_01931};
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931};
DE Short=GPATase {ECO:0000256|HAMAP-Rule:MF_01931};
GN Name=purF {ECO:0000256|HAMAP-Rule:MF_01931};
GN ORFNames=ECJG_02063 {ECO:0000313|EMBL:EGI20681.1};
OS Escherichia coli M718.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=656419 {ECO:0000313|EMBL:EGI20681.1, ECO:0000313|Proteomes:UP000002790};
RN [1] {ECO:0000313|EMBL:EGI20681.1, ECO:0000313|Proteomes:UP000002790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M718 {ECO:0000313|EMBL:EGI20681.1,
RC ECO:0000313|Proteomes:UP000002790};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Escherichia coli M718.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-
CC Rule:MF_01931}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-
CC phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine;
CC Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01931,
CC ECO:0000256|PIRSR:PIRSR000485-2};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01931,
CC ECO:0000256|PIRSR:PIRSR000485-2};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 1/2. {ECO:0000256|ARBA:ARBA00005209,
CC ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000256|ARBA:ARBA00010138,
CC ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01931}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL884129; EGI20681.1; -; Genomic_DNA.
DR RefSeq; WP_000334220.1; NZ_GL884129.1.
DR AlphaFoldDB; F4TH01; -.
DR SMR; F4TH01; -.
DR GeneID; 75172440; -.
DR HOGENOM; CLU_022389_2_1_6; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000002790; Unassembled WGS sequence.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR CDD; cd00715; GPATase_N; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR HAMAP; MF_01931; PurF; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005854; PurF.
DR InterPro; IPR035584; PurF_N.
DR NCBIfam; TIGR01134; purF; 1.
DR PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF13522; GATase_6; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_01931};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRSR:PIRSR000485-
KW 2};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01931,
KW ECO:0000256|PIRSR:PIRSR000485-2};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01931};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01931,
KW ECO:0000256|PIRNR:PIRNR000485}.
FT DOMAIN 2..236
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT ACT_SITE 2
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-1"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-2"
FT BINDING 367
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-2"
FT BINDING 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-2"
SQ SEQUENCE 505 AA; 56488 MW; 50FD08EA85E6F2A8 CRC64;
MCGIVGIAGV MPVNQSIYDA LTVLQHRGQD AAGIITIDAN NCFRLRKANG LVSDVFEARH
MQRLQGNMGI GHVRYPTAGS SSASEAQPFY VNSPYGITLA HNGNLTNAHE LRKKLFEEKR
RHINTTSDSE ILLNIFASEL DNFRHYPLEA DNIFAAIAAT NRLIRGAYAC VAMIIGHGMV
AFRDPNGIRP LVLGKRDIDE NRTEYMVASE SVALDTLGFD FLRDVAPGEA IYITEEGQLF
TRQCADNPVS NPCLFEYVYF ARPDSFIDKI SVYSARVNMG TKLGEKIARE WEDLDIDVVI
PIPETSCDIA LEIARILGKP YRQGFVKNRY VGRTFIMPGQ QLRRKSVRRK LNANRAEFRD
KNVLLVDDSI VRGTTSEQII EMAREAGAKK VYLASAAPEI RFPNVYGIDM PSATELIAHG
REVDEIRQII GADGLIFQDL NDLIDAVRAE NPDIQQFECS VFNGVYVTKD VDQGYLDFLD
TLRNDDAKAV QRQNEVENLE MHNEG
//
